71448-16-3

Basic information

• Product Name: Cbz-L-Phe-L-Lys-OH
• Synonyms: Cbz-L-Phe-L-Lys-OH
• CAS NO: 71448-16-3
• Molecular Weight: 427.5
• Mol File: 71448-16-3.mol

Chemical Properties

• CAS DataBase Reference: Cbz-L-Phe-L-Lys-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Cbz-L-Phe-L-Lys-OH(71448-16-3)
• EPA Substance Registry System: Cbz-L-Phe-L-Lys-OH(71448-16-3)

Safety Data

• Hazardous Substances Data: 71448-16-3(Hazardous Substances Data)

Upstream product

• 56-87-1 L-lysine 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 2418-95-3 (S)-2-amino-6-(tert-butoxycarbonylamino)hexanoic acid 
• 159857-90-6 N-Cbz-Phe-Lys(ε-Alloc)-4-aminobenzyl 4-nitrophenyl carbonate 
• 159857-89-3 N-Cbz-Phe-Lys(ε-Alloc)-4-aminobenzyl alcohol 
• 159857-88-2 N-Cbz-Phe-Lys(ε-Alloc)OH 
• 501-53-1 benzyl chloroformate 
• 63-91-2 L-phenylalanine 
• 6298-03-9 (2S)-2-amino-6-{[(prop-2-en-1-yloxy)carbonyl]amino}hexanoic acid 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 
• 1279111-11-3 C₅₅H₆₁N₅O₁₃ 
• 1279111-12-4 C₅₅H₆₀FN₅O₁₃ 
• 1279111-09-9 Benzyloxycarbonyl-L-phenylalanyl-L-lysyl-PABC-4-fluorodeacetylcolchicine 
• 1279111-08-8 Benzyloxycarbonyl-L-phenylalanyl-L-lysyl-PABC-deacetylcolchicine 

Downstream Products

• 1173817-69-0 Cbz-L-Phe-L-Lys-Bt 
• 6456-72-0 L-Phe-L-Lys 

Relevant articles and documents

RADIOPHARMACEUTICALS AND METHODS OF USE THEREOF

Targeted pharmaceuticals, particularly targeted radiopharmaceuticals, are provided which possess extended tumor retention time.

Increasing time on target: utilization of inhibitors of cysteine cathepsins to enhance the tumor retention of receptor-targeted agents

We report a strategy of utilizing irreversible cysteine cathepsin inhibitor as trapping agent to increase the tumor residence time of receptor-targeted agents. The targeted constructs incorporating these cysteine cathepsin trapping agents were able to for

Design, synthesis, and antitumor activity of 4-halocolchicines and their pro-drugs activated by cathepsin B

Novel colchicine derivatives possessing various substituents at the C4 position were prepared. Among them, 4-halo derivatives 3-6 were found to exhibit higher activity against cancer cell lines (A549, HT29, HCT116) as well as on mice transplanted with the HCT116 human colorectal carcinoma cell line than colchicine (1). Further, utilizing the 4-substituted colchicines, we prepared pro-drugs having a dipeptide side chain and demonstrated that these pro-drugs were activated by cathepsin B, an enzyme overexpressed in tumor cells, and exhibited selective toxicity to the tumor cells.

Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases

Dipeptidyl (acyloxy)methyl ketones (AOMKs) have been identified as mechanism-based inhibitors of certain cysteine proteases. These compounds are also inhibitors of the integral membrane proteins Rce1p and Ste24p, which are proteases that independently mediate a cleavage step associated with the maturation of certain isoprenylated proteins. The enzymatic mechanism of Rce1p is ill-defined, whereas Ste24p is a zinc metalloprotease. Rce1p is required for the proper processing of the oncoprotein Ras and is viewed as a potential target for cancer therapy. In this study, we synthesized a small library of dipeptidyl AOMKs to investigate the structural elements that contribute to the inhibitor properties of this class of molecules toward Rce1p and Ste24p. The compounds were evaluated using a fluorescence-based in vitro proteolysis assay. The most potent dipeptidyl AOMKs contained an arginine residue and the identity of the benzoate group strongly influenced potency. A 'warhead' free AOMK inhibited Rce1p and Ste24p. The data suggest that the dipeptidyl AOMKs are not mechanism-based inhibitors of Rce1p and Ste24p and corroborate the hypothesis that Rce1p is not a cysteine protease.

Convenient synthesis of C-terminal di- and tri-peptide amides from N-protected dipeptidoylbenzotriazoles

N-Protected dipeptidoylbenzotriazoles react with aqueous ammonia to give dipeptide primary amides (77-98%) and with N-unprotected α-amino amides to afford tripeptide primary amides (82-86%).

Characteristics of chymotrypsin modified with water-soluble acylating reagents and its peptide synthesis ability in aqueous organic media.

Several kinds of modified chymotrypsin were prepared with water-soluble acylating reagents, and their characteristics after hydrolyzing with unmodified chymotrypsin in aqueous-N,N'-dimethylformamide (DMF) media were compared. It was found that chymotrypsi